Amino acid sequences of the tryptic peptides from carboxymethylated L-asparaginase from Escherichia coli

Hoppe-Seyler's Zeitschrift für physiologische Chemie
T MaitaG Matsuda


S-Carboxymethylated L-asparaginase was digested with trypsin and the resulting peptides were isolated by using gel filtration, ion exchange column chromatography and paper chromatography. Among the peptides thus isolated, 27 peptides were considered not to overlap and the sum of the amino acids from these 27 peptides is in good agreement with amino acid composition of the enzyme. The amino acid sequences of the peptides were determined by fragmentation with various enzymes and subtractive Edman degradation.


Jan 1, 1987·Proceedings of the National Academy of Sciences of the United States of America·T MaitaG Matsuda
Mar 17, 2007·Critical Reviews in Biotechnology·Neelam VermaSneh Anand
Jan 1, 1980·Hoppe-Seyler's Zeitschrift für physiologische Chemie·T Maita, G Matsuda
Nov 1, 1981·Hoppe-Seyler's Zeitschrift für physiologische Chemie·T MaitaK Takahashi
Oct 1, 1986·Biological Chemistry Hoppe-Seyler·B WatanabeG Matsuda
Jan 1, 1981·European Journal of Biochemistry·T MaitaG Matsuda
Feb 1, 1986·Biological Chemistry Hoppe-Seyler·Y TaniokaG Matsuda


Dec 1, 1974·Journal of Biochemistry·T MaitaG Matsuda
Feb 1, 1970·Hoppe-Seyler's Zeitschrift für physiologische Chemie·A ArensW Kaufmann
May 1, 1964·Archives of Biochemistry and Biophysics·L T MASHBURN, J C WRISTON

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